Fig. 2: The teneurin-3 A1B1 compact dimer interface comprises three distinct interaction sites.
From: Alternative splicing controls teneurin-3 compact dimer formation for neuronal recognition
A Density map of the Ten3-A1B1 compact dimer with domains that participate in the interfaces shown in colour. The colour code is shown below panel B, along with the interface area (IA) per domain. B Open book representation of the density map. The left subunit shows the participating domains in colour, and the right subunit displays the specific interface residues. Fill colours indicate the domains in which the residues are located, and outline colours indicate the domains in which the contacting residues reside. C Schematic representation of EGF8-ABD interface in the compact dimer versus the ABD domain of a Ten3 A1B1 non-compact subunit reconstruction. Residues 2579-2588 are displaced or disordered in the compact dimer form, and residues 2582-2587 form β-strand 5 in ABD of the non-compact subunit. D Close-up of interface I, the EGF8-ABD extended β-sheet (PDB:8R50). Resolved residues from insert A (labelled A) are coloured orange E Open book surface hydrophobicity representation of the EGF8-ABD interface. F Close-up of interface II, comprising YD-ABD contacts. G Close-up of interface III, the YD-YD and YD-ABD contacts. In the close-ups, ionic bonds are indicated in dashed yellow lines and hydrogen bonds in dashed blue lines, and transparent surface representation is used to distinguish between subunits within the compact dimer. Only residues with >5% per-residue buried surface area are represented. For clarity, Leu2530, Ser2596, and Arg 2624 are not displayed.
